ID   SHTX5_STIHA             Reviewed;          86 AA.
AC   B1B5J0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=OMEGA-stichotoxin-Shd4a {ECO:0000303|PubMed:22683676};
DE            Short=OMEGA-SHTX-Shd4a {ECO:0000303|PubMed:22683676};
DE   AltName: Full=EGF-like peptide SHTX V {ECO:0000303|PubMed:18243416};
DE   AltName: Full=SHTX-5;
DE   Flags: Precursor;
OS   Stichodactyla haddoni (Saddle carpet anemone) (Haddon's sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Stichodactylidae; Stichodactyla.
OX   NCBI_TaxID=475174;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18243416; DOI=10.1016/j.peptides.2007.12.010;
RA   Honma T., Kawahata S., Ishida M., Nagai H., Nagashima Y., Shiomi K.;
RT   "Novel peptide toxins from the sea anemone Stichodactyla haddoni.";
RL   Peptides 29:536-544(2008).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=22683676; DOI=10.1016/j.toxicon.2012.05.020;
RA   Oliveira J.S., Fuentes-Silva D., King G.F.;
RT   "Development of a rational nomenclature for naming peptide and protein
RT   toxins from sea anemones.";
RL   Toxicon 60:539-550(2012).
CC   -!- FUNCTION: Has both toxic and EGF activity. Its EGF activity consists of
CC       rounding cells (morphological change) and inducing tyrosine
CC       phosphorylation of the EGFR in A431 cells, but with a lower potency
CC       that human EGF. {ECO:0000250|UniProtKB:Q76CA1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Nematocyst {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the EGF domain peptide family. {ECO:0000305}.
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DR   EMBL; AB362571; BAG12826.1; -; mRNA.
DR   AlphaFoldDB; B1B5J0; -.
DR   SMR; B1B5J0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000742; EGF-like_dom.
DR   Pfam; PF00008; EGF; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; EGF-like domain;
KW   Nematocyst; Secreted; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..36
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000344520"
FT   CHAIN           39..86
FT                   /note="OMEGA-stichotoxin-Shd4a"
FT                   /id="PRO_0000344521"
FT   DOMAIN          40..82
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        44..59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        53..70
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DISULFID        72..81
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   86 AA;  9558 MW;  74A83EFAF41EAD2A CRC64;
     MASFRTLFAC VVILCCVLWS SMARYGEDME VETEMNKRDE GVRCTGQHAS SFCLNGGTCR
     HIASLGEYYC ICPGDYTGHR CDQKSG